Evidence map›Paper›PMID 32801776›Full record

ArticleOncoTargets and therapy2020

Phosphoribosyl Pyrophosphate Amidotransferase Promotes the Progression of Thyroid Cancer via Regulating Pyruvate Kinase M2.

Bing Liu, Meiyue Song, Huadong Qin, Bin Zhang, Yao Liu, Yu Sun, Yanfei Ma, Tiefeng Shi

Open access · goldAbstract read
In one paragraph

Article in OncoTargets and therapy, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.8field-weighted citation impact, top 34% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 18 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Bing Liu *The 4th Department of General Surgery, The Second Affiliated Hospital of Harbin Medical University, Harbin City 150086, Heilongjiang Province, People's Republic of China.
Meiyue Song *The Pathology Department, The Second Affiliated Hospital of Harbin Medical University, Harbin City 150086, Heilongjiang Province, People's Republic of China.
Huadong QinThe 4th Department of General Surgery, The Second Affiliated Hospital of Harbin Medical University, Harbin City 150086, Heilongjiang Province, People's Republic of China.
Bin ZhangThe 4th Department of General Surgery, The Second Affiliated Hospital of Harbin Medical University, Harbin City 150086, Heilongjiang Province, People's Republic of China.
Yao LiuThe 4th Department of General Surgery, The Second Affiliated Hospital of Harbin Medical University, Harbin City 150086, Heilongjiang Province, People's Republic of China.
Yu SunThe 4th Department of General Surgery, The Second Affiliated Hospital of Harbin Medical University, Harbin City 150086, Heilongjiang Province, People's Republic of China.
Yanfei MaThe 4th Department of General Surgery, The Second Affiliated Hospital of Harbin Medical University, Harbin City 150086, Heilongjiang Province, People's Republic of China.
Tiefeng ShiThe 4th Department of General Surgery, The Second Affiliated Hospital of Harbin Medical University, Harbin City 150086, Heilongjiang Province, People's Republic of China.ORCID 0000-0001-9443-0711
Harbin Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPyruvate kinase is an enzyme that catalyzes the conversion of phosphoenolpyruvate and ADP to pyruvate and ATP in glycolysis and plays a role in regulating cell metabolism. It is reported that the activity of pyruvate kinase is increased in cancers. Phosphoribosyl amidotransferase (PPAT) is reported to be a crucial regulator for pyruvate kinase activity in lung cancer. However, its role in thyroid cancer remains largely unknown. MATERIALS AND

methodsImmunohistochemical analysis and qRT-PCR were used to detect the expression of PPAT in thyroid cancer samples. Both gain-of-function and loss-of-function models were constructed in thyroid cancer cell lines and the biological functions of PPAT on cellular phenotypes were studied using CCK-8 assay and transwell assay in vitro, respectively. Then, Western blot was used to evaluate the change of PKM2 and downstream signal pathways after PPAT was overexpressed or knocked down.

resultsImmunohistochemical analysis showed increased expression of PPAT in thyroid cancer tissues, and it was associated with unfavorable pathological characteristics. Knockdown and overexpression assays suggested that altering PPAT expression modulated cell proliferation, migration, and invasion. In terms of mechanism, PPAT could positively regulate the expression of PKM2 and activate ERK and STAT3 signaling pathways.

conclusionPPAT plays crucial roles in regulating proliferation, migration, and invasion of thyroid cancer cells via activating PKM2, ERK, and STAT3.

Indexed as

invasionmigrationPKM2PPATproliferationthyroid cancer

Identifiers

PMID32801776
PMCPMC7413720
OpenAlexW3046270643

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.